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O00418 (EF2K_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic elongation factor 2 kinase

Short name=eEF-2 kinase
Short name=eEF-2K
EC=2.7.11.20
Alternative name(s):
Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase
Gene names
Name:EEF2K
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. Ref.1 Ref.8

Catalytic activity

ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate. Ref.1

Enzyme regulation

Undergoes calcium/calmodulin-dependent intramolecular autophosphorylation, and this results in it becoming partially calcium/calmodulin-independent By similarity.

Subunit structure

Monomer or homodimer Potential.

Domain

The catalytic domain is located to N-terminal region. The neighbor region contains the calmodulin-binding domain. Ref.4

Post-translational modification

Autophosphorylated at multiple residues, Thr-348 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-398 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-78 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis. Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-359 or RPS6KA1 and RPS6KB1 at Ser-366 instead decrease EEF2K activity and promote protein synthesis. Ref.4 Ref.5 Ref.6 Ref.8 Ref.11 Ref.17 Ref.19

Sequence similarities

Belongs to the protein kinase superfamily. Alpha-type protein kinase family.

Contains 1 alpha-type protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.20
Chain2 – 725724Eukaryotic elongation factor 2 kinase
PRO_0000086936

Regions

Domain116 – 326211Alpha-type protein kinase
Nucleotide binding296 – 3027ATP By similarity
Region594 – 61017Calmodulin-binding Potential
Region610 – 62718Pseudosubstrate/autoinhibitory domain Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.20
Modified residue181Phosphoserine Ref.7 Ref.9 Ref.10 Ref.14 Ref.15 Ref.18
Modified residue611Phosphoserine; by autocatalysis Ref.19
Modified residue661Phosphoserine; by autocatalysis Ref.19
Modified residue711Phosphoserine By similarity
Modified residue781Phosphoserine; by autocatalysis and TRPM7 Ref.17 Ref.19
Modified residue3481Phosphothreonine; by autocatalysis Ref.12 Ref.15 Ref.19
Modified residue3531Phosphothreonine; by autocatalysis Ref.19
Modified residue3591Phosphoserine; by MAPK13 and CDK1 Ref.5 Ref.11
Modified residue3661Phosphoserine; by autocatalysis, RPS6KA1 and RPS6KB1 Ref.6 Ref.19
Modified residue3981Phosphoserine; by AMPK Ref.8
Modified residue4451Phosphoserine; by autocatalysis Ref.10 Ref.15 Ref.19
Modified residue4701Phosphoserine Ref.12 Ref.15 Ref.18
Modified residue4741Phosphoserine; by autocatalysis Ref.9 Ref.12 Ref.15 Ref.19
Modified residue4771Phosphoserine Ref.12
Modified residue4911Phosphoserine; by autocatalysis Ref.19
Modified residue5001Phosphoserine; by PKA By similarity

Natural variations

Natural variant231H → R. Ref.3 Ref.21
Corresponds to variant rs9935059 [ dbSNP | Ensembl ].
VAR_033915
Natural variant751P → A. Ref.21
Corresponds to variant rs17841292 [ dbSNP | Ensembl ].
VAR_033916
Natural variant2911T → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.21
VAR_041534
Natural variant3611Q → R. Ref.1 Ref.3
Corresponds to variant rs4783453 [ dbSNP | Ensembl ].
VAR_058405
Natural variant4331R → W. Ref.21
Corresponds to variant rs56137739 [ dbSNP | Ensembl ].
VAR_041535
Natural variant6091D → H. Ref.21
VAR_041536

Experimental info

Mutagenesis781S → A: Decreased kinase activity. Ref.19
Mutagenesis3481T → A: Decreased kinase activity. Ref.19
Mutagenesis3661S → A: Abrogates phosphorylation by RPS6KB1. Ref.6 Ref.19
Mutagenesis3661S → A: Decreased kinase activity. Ref.6 Ref.19

Sequences

Sequence LengthMass (Da)Tools
O00418 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 9D2900E50EFF12DA

FASTA72582,144
        10         20         30         40         50         60 
MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPSSNQ NVNSKVNKYY 

        70         80         90        100        110        120 
SNLTKSERYS SSGSPANSFH FKEAWKHAIQ KAKHMPDPWA EFHLEDIATE RATRHRYNAV 

       130        140        150        160        170        180 
TGEWLDDEVL IKMASQPFGR GAMRECFRTK KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV 

       190        200        210        220        230        240 
YFEDVRLQME AKLWGEEYNR HKPPKQVDIM QMCIIELKDR PGKPLFHLEH YIEGKYIKYN 

       250        260        270        280        290        300 
SNSGFVRDDN IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL 

       310        320        330        340        350        360 
GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL RGTEEKCGSP 

       370        380        390        400        410        420 
QVRTLSGSRP PLLRPLSENS GDENMSDVTF DSLPSSPSSA TPHSQKLDHL HWPVFSDLDN 

       430        440        450        460        470        480 
MASRDHDHLD NHRESENSGD SGYPSEKRGE LDDPEPREHG HSYSNRKYES DEDSLGSSGR 

       490        500        510        520        530        540 
VCVEKWNLLN SSRLHLPRAS AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC 

       550        560        570        580        590        600 
EKGEEWDQES AVFHLEHAAN LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY 

       610        620        630        640        650        660 
LLKAAEAGDR QSMILVARAF DSGQNLSPDR CQDWLEALHW YNTALEMTDC DEGGEYDGMQ 

       670        680        690        700        710        720 
DEPRYMMLAR EAEMLFTGGY GLEKDPQRSG DLYTQAAEAA MEAMKGRLAN QYYQKAEEAW 


AQMEE 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase."
Ryazanov A.G., Ward M.D., Mendola C.E., Pavur K.S., Dorovkov M.V., Wiedmann M., Erdjument-Bromage H., Tempst P., Parmer T.G., Prostko C.R., Germino F.J., Hait W.N.
Proc. Natl. Acad. Sci. U.S.A. 94:4884-4889(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, VARIANT ARG-361.
Tissue: Glial tumor.
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-23 AND ARG-361.
Tissue: Lymph.
[4]"Mapping the functional domains of elongation factor-2 kinase."
Pavur K.S., Petrov A.N., Ryazanov A.G.
Biochemistry 39:12216-12224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION, DOMAIN.
[5]"A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta."
Knebel A., Morrice N., Cohen P.
EMBO J. 20:4360-4369(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-359.
[6]"Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase."
Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.
EMBO J. 20:4370-4379(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-366 BY RPS6KA1 AND RPS6KB1, MUTAGENESIS OF SER-366.
[7]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398."
Browne G.J., Finn S.G., Proud C.G.
J. Biol. Chem. 279:12220-12231(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-398.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"cdc2-cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner."
Smith E.M., Proud C.G.
EMBO J. 27:1005-1016(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-359.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348; SER-470; SER-474 AND SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-348; SER-445; SER-470 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The channel-kinase TRPM7 regulates phosphorylation of the translational factor eEF2 via eEF2-k."
Perraud A.L., Zhao X., Ryazanov A.G., Schmitz C.
Cell. Signal. 23:586-593(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-78.
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase."
Pyr Dit Ruys S., Wang X., Smith E.M., Herinckx G., Hussain N., Rider M.H., Vertommen D., Proud C.G.
Biochem. J. 442:681-692(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-61; SER-66; SER-78; THR-348; THR-353; SER-366; SER-445; SER-474 AND SER-491, MUTAGENESIS OF SER-78; THR-348 AND SER-366.
[20]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[21]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-23; ALA-75; MET-291; TRP-433 AND HIS-609.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U93850 mRNA. Translation: AAB58270.1.
AC009034 Genomic DNA. No translation available.
BC032665 mRNA. Translation: AAH32665.1.
CCDSCCDS10604.1.
RefSeqNP_037434.1. NM_013302.3.
XP_005276554.1. XM_005276497.1.
UniGeneHs.498892.

3D structure databases

ProteinModelPortalO00418.
SMRO00418. Positions 117-323, 527-645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118953. 144 interactions.
IntActO00418. 10 interactions.
MINTMINT-207181.
STRING9606.ENSP00000263026.

Chemistry

BindingDBO00418.
ChEMBLCHEMBL5026.
GuidetoPHARMACOLOGY2014.

PTM databases

PhosphoSiteO00418.

Proteomic databases

MaxQBO00418.
PaxDbO00418.
PRIDEO00418.

Protocols and materials databases

DNASU29904.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263026; ENSP00000263026; ENSG00000103319.
GeneID101930123.
29904.
KEGGhsa:101930123.
hsa:29904.
UCSCuc002dki.3. human.

Organism-specific databases

CTD29904.
GeneCardsGC16P022217.
HGNCHGNC:24615. EEF2K.
HPACAB007818.
MIM606968. gene.
neXtProtNX_O00418.
PharmGKBPA134992891.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145133.
HOGENOMHOG000022023.
HOVERGENHBG002318.
InParanoidO00418.
KOK08292.
OMAQIHTETG.
OrthoDBEOG7673B0.
PhylomeDBO00418.
TreeFamTF316085.

Enzyme and pathway databases

BRENDA2.7.11.20. 2681.
ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressO00418.
BgeeO00418.
CleanExHS_EEF2K.
GenevestigatorO00418.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR017400. Elongation_factor_2_kinase.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR006597. Sel1-like.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF02816. Alpha_kinase. 1 hit.
PF08238. Sel1. 4 hits.
[Graphical view]
PIRSFPIRSF038139. Elongation_factor_2_kinase. 1 hit.
SMARTSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiEEF2K.
NextBio52478.
PROO00418.
SOURCESearch...

Entry information

Entry nameEF2K_HUMAN
AccessionPrimary (citable) accession number: O00418
Secondary accession number(s): Q8N588
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM